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Overview for MACiE Entry M0187

Version history

General Information

EC Number: 5.1.2.2 (A member of the Isomerases, Racemases and epimerases, Acting on hydroxy acids and derivatives)

Enzyme Name: mandelate racemase

Biological Species: Pseudomonas putida (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

Representative PDB Code: 1mns - ON THE ROLE OF LYSINE 166 IN THE MECHANISM OF MANDELATE RACEMASE FROM PSEUDOMONAS PUTIDA: MECHANISTIC AND CRYSTALLOGRAPHIC EVIDENCE FORSTEREOSPECIFIC ALKYLATION BY (R)-ALPHA-PHENYLGLYCIDATE (Resolution = 2.00 Å).

Catalytic CATH Codes:

"Other" CATH Codes:

Display structure information

Overall Reaction:

Image of (S)-mandelate

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Image of (R)-mandelate

(S)-mandelate
C01984
CHEBI:17756
(R)-mandelate
C01983
CHEBI:32382

Overall Comment: The mechanism shown in the following steps refers to the direction shown in overall reaction not in the reverse direction. Lys166 is the (S)-specific acid/base catalyst and His297 is the (R)-specific acid/base catalyst, thus in the reverse reaction, His297 deprotonates the (R)-mandelate and the intermediate is reprotonated from Lys166.


View similar reactions


Stepwise Description of the Reaction

Step 1Lys166 deprotonates the (S)-mandelate substrate, which results in a keto-enol tautomerisation.
Step 2The intermediate undergoes another keto-enol tautomerisation which reprotonates the intermediate from His297.
Step 3His297 deprotonates water, which deprotonates Lys166 in an inferred return step.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Lys 164 A Side Chain
Lys 166 A Side Chain
Asp 270 A Side Chain
His 297 A Side Chain
Glu 317 A Side Chain

Metal Cofactors for M0187

Type Het group Number Chain
magnesium MG 360 x Overview

References

  1. J. A. Gerlt et al. (1993), J. Am. Chem. Soc., 115, 11552-11568. An explanation for rapid enzyme-catalyzed proton abstraction from carbon acids: importance of late transition states in concerted mechanisms.
  2. S. L. Schafer et al. (1996), Biochemistry, 35, 5662-5669. Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the D270N mutant.
    Medline: 8639525
  3. M. Garcia-Viloca et al. (2001), J. Am. Chem. Soc., 123, 709-721. A QM/MM study of the racemization of vinylglycolate catalyzed by mandelate racemase enzyme.
    Medline: 11456585

Homologue information for M0187 (1mns)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with at least one Catalytic CATH code in common (different mechanisms):

MACiE Entry Enzyme Name
EC Number
PDB code CATH code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0311 phosphopyruvate hydratase
4.2.1.11
7enl 3.20.20.120
3.30.390.10
0.55550.6079Compare
M0269 muconate cycloisomerase
5.5.1.1
1muc 3.20.20.120
3.30.390.10
0.520.6427Compare

View a comparison of the other reactions in MACiE with the CATH domain 3.20.20.120

View a comparison of the other reactions in MACiE with the CATH domain 3.30.390.10


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to EzCatDB Link to SFLD

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catalytic activity (molecular function)
metabolic process (biological process)
cellular amino acid catabolic process (biological process)
isomerase activity (molecular function)
mandelate racemase activity (molecular function)
mandelate metabolic process (biological process)
metal ion binding (molecular function)
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